ID   A0A2G5WMS3_9BACL        Unreviewed;      1015 AA.
AC   A0A2G5WMS3;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   22-FEB-2023, entry version 20.
DE   RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=CSV79_02975 {ECO:0000313|EMBL:PIC65246.1};
OS   Sporosarcina sp. P13.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX   NCBI_TaxID=2048263 {ECO:0000313|EMBL:PIC65246.1, ECO:0000313|Proteomes:UP000229993};
RN   [1] {ECO:0000313|EMBL:PIC65246.1, ECO:0000313|Proteomes:UP000229993}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P13 {ECO:0000313|EMBL:PIC65246.1,
RC   ECO:0000313|Proteomes:UP000229993};
RA   Oliver A., Kay M., Cooper K.;
RT   "Comparative genomics and methylomics between geographically and
RT   phenotypically diverse Sporosarcina species.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC         Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:173112; EC=2.7.7.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00024632};
CC   -!- SUBUNIT: DNA polymerase III contains a core (composed of alpha, epsilon
CC       and theta chains) that associates with a tau subunit. This core
CC       dimerizes to form the POLIII' complex. PolIII' associates with the
CC       gamma complex (composed of gamma, delta, delta', psi and chi chains)
CC       and with the beta chain to form the complete DNA polymerase III
CC       complex. {ECO:0000256|ARBA:ARBA00026073}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PIC65246.1}.
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DR   EMBL; PDYM01000003; PIC65246.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5WMS3; -.
DR   EnsemblBacteria; PIC65246; PIC65246; CSV79_02975.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000229993; Unassembled WGS sequence.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd04485; DnaE_OBF; 1.
DR   Gene3D; 1.10.150.870; -; 1.
DR   Gene3D; 1.10.10.1600; Bacterial DNA polymerase III alpha subunit, thumb domain; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR   InterPro; IPR041931; DNA_pol3_alpha_thumb_dom.
DR   InterPro; IPR040982; DNA_pol3_finger.
DR   InterPro; IPR029460; DNAPol_HHH.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   InterPro; IPR004013; PHP_dom.
DR   InterPro; IPR004805; PolC_alpha.
DR   PANTHER; PTHR32294; DNA POLYMERASE III SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR32294:SF0; DNA POLYMERASE III SUBUNIT ALPHA; 1.
DR   Pfam; PF07733; DNA_pol3_alpha; 1.
DR   Pfam; PF17657; DNA_pol3_finger; 1.
DR   Pfam; PF14579; HHH_6; 1.
DR   Pfam; PF02811; PHP; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   TIGRFAMs; TIGR00594; polc; 1.
PE   4: Predicted;
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          14..121
FT                   /note="PHP"
FT                   /evidence="ECO:0000259|Pfam:PF02811"
FT   DOMAIN          274..527
FT                   /note="Bacterial DNA polymerase III alpha subunit NTPase"
FT                   /evidence="ECO:0000259|Pfam:PF07733"
FT   DOMAIN          530..692
FT                   /note="DNA polymerase III alpha subunit finger"
FT                   /evidence="ECO:0000259|Pfam:PF17657"
FT   DOMAIN          766..850
FT                   /note="DNA polymerase helix-hairpin-helix motif"
FT                   /evidence="ECO:0000259|Pfam:PF14579"
FT   DOMAIN          944..1011
FT                   /note="OB"
FT                   /evidence="ECO:0000259|Pfam:PF01336"
SQ   SEQUENCE   1015 AA;  114943 MW;  A935285B9FE563EF CRC64;
     MNLMYPQIIT GADLLRGIVK LDELAPLLKE RGASSAAIVN SKLFGVRSFS TMLSKYGIRP
     VIGLSVKVSI ADEDLLVYIY AQNQEGFSNL LKISSAISTR EEGNLPLSWL QAYRQSCFVV
     CALTHASWTN HRNVEVLQQL AEDVKQSTFI GISRPGGARH TKEDNIIQLS EECELSIVAC
     HEARFLHADD FPAYEVATAI RKGYKLNDSK KPKNRFRQAY LPTQKTFSEW FADHPEWLQK
     MADLLDSCEV KFGKEPFQLP KFPVQEGQTP IRLLTEKCQD GLAKRFQSMP IEYAERLRYE
     LTIIEQMGFT DYFLIVEDYV RYAKSQQILV GPGRGSSAGS LVAFALGITE VDPIQYGLLF
     ERFLNPERVT MPDIDIDFAD NRRTEVVNYV ADTYGKHYAA QIITFGTLST KAVARNVARV
     LDFTPEEVRF MSSELNSGLS FSETIRQSKK LQDWMAVDPR RARWREAAER LEDLPRNAST
     HAAGVVLAAN PLVNYVPLQI GTDEVFLTQW AMKDVEEAGL LKMDFLGLRN LTLLDRIRSM
     IEYNNKQPIN FEEIPLDDQR TYRLFKAGDM SGIFQFESPG MRRALQTIQP DNFKDLYSVN
     ALYRPGPMEF IPLYSRRKNG QEQTNYDIPE LQPILAETYG IIIYQEQIMK IAVEIAGFTM
     SEADLLRRAI SKKNQQVLEQ ERQHFIAGAT KKGFDHVKAN NVYNLIVKFA DYGFPKSHAV
     AYTLISYRLA FFKANEPNIF YAAYLSSLSG NKEKTVELIR EIKAKGIEVY PPSVKSSRYS
     HTVEGNAIRL GLGVIKGVTY PFYQQLAAAR GNWSSMFDMA ISLGANHFNE KSMIPLIKAG
     ALDEFGEKRS VLLASVDAAH SHALYIGNDA FSDQFQFNSR PKYTPGGAMD QMTLLSFERD
     VLGFYLSEHP VEQLKRNVMD HIQPIASLVN LRQGTKVKCI GLILSVKRIR TKKGEAMAFF
     TLQDETEEVS CTVFPKQYAN FSNLNENEFI QVTGSIEFRN QSLQLIIDKL VPVTS
//